Investigating the reversible inhibition model of laccase by hydrogen peroxide for bioelectrocatalytic applications

The reversible inhibition of laccase by H2O2 as a bioelectrocatalyst was studied in mediated- and direct electron transfer-based configurations to understand the differences in mechanism. The reversible inhibition of laccase follows a noncompetitive inhibition model when 2,2-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) is used as an electron mediator, whereas laccase is inhibited by an uncompetitive inhibition model when anthracene-moieties are used to intelligently "dock" laccase to electrodes (consisting of multi-walled carbon nanotubes, MWCNTs) which afford direct electron transfer (DET). This further confirms the efficient orientation of laccase onto suitably-designed docking moieties for bioelectrocatalysis applications.